UniProtKB - P42206 (GUDD_PSEPU)
Protein
Glucarate dehydratase
Gene
gudD
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Functioni
Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc).
Catalytic activityi
- EC:4.2.1.40
Cofactori
Mg2+By similarity
: D-glucarate degradation Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes 2,5-dioxopentanoate from D-glucarate.Proteins known to be involved in the 2 steps of the subpathway in this organism are:
- Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (CBP06_22880), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (BL240_24700), Glucarate dehydratase (B7H18_09755), Glucarate dehydratase (BGP80_00075), Glucarate dehydratase (DW66_4984), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD), Glucarate dehydratase (KF715C_ch52340), Glucarate dehydratase (B8W72_18600), Glucarate dehydratase (BGP84_21935), Glucarate dehydratase (SAMN03097715_01930), Glucarate dehydratase (B7H19_23370), Glucarate dehydratase (gudD), Glucarate dehydratase (gudD)
- Probable 5-dehydro-4-deoxyglucarate dehydratase (HA62_06375), Probable 5-dehydro-4-deoxyglucarate dehydratase (DW66_3364), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (BGP84_13810), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (PSEMO_05320), Probable 5-dehydro-4-deoxyglucarate dehydratase (AO269_10510), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (AYO28_18420), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (SAMN03097715_05359), Probable 5-dehydro-4-deoxyglucarate dehydratase (HB4184_13805), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (BGP80_16365), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (KF715C_ch30880), Probable 5-dehydro-4-deoxyglucarate dehydratase (B7H18_17750), Probable 5-dehydro-4-deoxyglucarate dehydratase (BL240_12265), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (BIW19_13625), 5-dehydro-4-deoxyglucarate dehydratase, Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (CBL13_00668), Probable 5-dehydro-4-deoxyglucarate dehydratase (mosA), Probable 5-dehydro-4-deoxyglucarate dehydratase (B8W72_02700), Probable 5-dehydro-4-deoxyglucarate dehydratase (kdgD), Probable 5-dehydro-4-deoxyglucarate dehydratase (mosA), Probable 5-dehydro-4-deoxyglucarate dehydratase (HB13667_24465)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2,5-dioxopentanoate from D-glucarate, the pathway D-glucarate degradation and in Carbohydrate acid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 38 | SubstrateBy similarity | 1 | |
Binding sitei | 109 | SubstrateBy similarity | 1 | |
Binding sitei | 156 | SubstrateBy similarity | 1 | |
Binding sitei | 211 | SubstrateBy similarity | 1 | |
Active sitei | 213 | Proton acceptorBy similarity | 1 | |
Metal bindingi | 241 | MagnesiumBy similarity | 1 | |
Metal bindingi | 272 | MagnesiumBy similarity | 1 | |
Metal bindingi | 295 | MagnesiumBy similarity | 1 | |
Binding sitei | 295 | SubstrateBy similarity | 1 | |
Active sitei | 345 | Proton acceptorBy similarity | 1 | |
Binding sitei | 374 | SubstrateBy similarity | 1 | |
Binding sitei | 427 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- glucarate dehydratase activity Source: UniProtKB-EC
- magnesium ion binding Source: InterPro
GO - Biological processi
- D-glucarate catabolic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Lyase |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-15627 |
BRENDAi | 4.2.1.40, 5092 |
SABIO-RKi | P42206 |
UniPathwayi | UPA00564;UER00627 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:gudD |
Organismi | Pseudomonas putida (Arthrobacter siderocapsulatus) |
Taxonomic identifieri | 303 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000171268 | 1 – 451 | Glucarate dehydrataseAdd BLAST | 451 |
Interactioni
Subunit structurei
Homotetramer.
1 PublicationStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P42206 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P42206 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 241 – 243 | Substrate bindingBy similarity | 3 | |
Regioni | 345 – 347 | Substrate bindingBy similarity | 3 |
Sequence similaritiesi
Family and domain databases
CDDi | cd03323, D-glucarate_dehydratase, 1 hit |
Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
InterProi | View protein in InterPro IPR036849, Enolase-like_C_sf IPR029017, Enolase-like_N IPR029065, Enolase_C-like IPR017653, Glucarate_dehydratase IPR034598, GlucD-like IPR013342, Mandelate_racemase_C IPR034593, Mandelate_racemase_DgoD-like IPR013341, Mandelate_racemase_N_dom |
PANTHERi | PTHR48080, PTHR48080, 1 hit |
Pfami | View protein in Pfam PF13378, MR_MLE_C, 1 hit PF02746, MR_MLE_N, 1 hit |
SMARTi | View protein in SMART SM00922, MR_MLE, 1 hit |
SUPFAMi | SSF51604, SSF51604, 1 hit SSF54826, SSF54826, 1 hit |
TIGRFAMsi | TIGR03247, glucar-dehydr, 1 hit |
i Sequence
Sequence statusi: Complete.
P42206-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEALNQSQAA TGAPVITDLK VVPVAGHDSM LLNLSGAHGP LFTRNILILT
60 70 80 90 100
DSSGHVGVGE VPGGEGIRKT LEDARHLLIN QSIGNYQSLL NKVRNAFADR
110 120 130 140 150
DVGGRGLQTF DLRIAVHAVT AVESALLDLL GQHLQVPVAA LLGEGQQRDA
160 170 180 190 200
VEMLGYLFYV GDRNKTDLGY RSEHEADNEW FRLRNKEALT PESVVALAEA
210 220 230 240 250
AYDRYGFKDF KLKGGVLRGE DEIAAVTALS ERFPDARITL DPNGAWSLKE
260 270 280 290 300
AVALCRDQHH VLAYAEDPCG AENGYSGREV MAEFRRSTGL RTATNMIATD
310 320 330 340 350
WRQMGHAIQL QSVDIPLADP HFWTMQGSVR VAQMCNEWGL TWGSHSNNHF
360 370 380 390 400
DISLAMFTHV AAAAPGNITA IDTHWIWQDG QRLTKEPLQI KGGLVEVPKK
410 420 430 440 450
PGLGVELDWD ALMKAHEVYK SMGLGARDDA TAMRYLVSGW EFNNKRPCMV
R
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M69160 Genomic DNA Translation: AAA25868.1 |
PIRi | S27617 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M69160 Genomic DNA Translation: AAA25868.1 |
PIRi | S27617 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BQG | X-ray | 2.30 | A | 1-451 | [»] | |
SMRi | P42206 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Enzyme and pathway databases
UniPathwayi | UPA00564;UER00627 |
BioCyci | MetaCyc:MONOMER-15627 |
BRENDAi | 4.2.1.40, 5092 |
SABIO-RKi | P42206 |
Miscellaneous databases
EvolutionaryTracei | P42206 |
Family and domain databases
CDDi | cd03323, D-glucarate_dehydratase, 1 hit |
Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
InterProi | View protein in InterPro IPR036849, Enolase-like_C_sf IPR029017, Enolase-like_N IPR029065, Enolase_C-like IPR017653, Glucarate_dehydratase IPR034598, GlucD-like IPR013342, Mandelate_racemase_C IPR034593, Mandelate_racemase_DgoD-like IPR013341, Mandelate_racemase_N_dom |
PANTHERi | PTHR48080, PTHR48080, 1 hit |
Pfami | View protein in Pfam PF13378, MR_MLE_C, 1 hit PF02746, MR_MLE_N, 1 hit |
SMARTi | View protein in SMART SM00922, MR_MLE, 1 hit |
SUPFAMi | SSF51604, SSF51604, 1 hit SSF54826, SSF54826, 1 hit |
TIGRFAMsi | TIGR03247, glucar-dehydr, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GUDD_PSEPU | |
Accessioni | P42206Primary (citable) accession number: P42206 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1995 | |
Last modified: | February 10, 2021 | |
This is version 96 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families